Molecular mechanism of histone variant H2A.B on stability and assembly of nucleosome and chromatin structures.

ABSTRACT:

Background

H2A.B, the most divergent histone variant of H2A, can significantly modulate nucleosome and chromatin structures. However, the related structural details and the underlying mechanism remain elusive to date. In this work, we built atomic models of the H2A.B-containing nucleosome core particle (NCP), chromatosome, and chromatin fiber. Multiscale modeling including all-atom molecular dynamics and coarse-grained simulations were then carried out for these systems.

Results

It is found that sequence differences at the C-terminal tail, the docking domain, and the L2 loop, between H2A.B and H2A are directly responsible for the DNA unwrapping in the H2A.B NCP, whereas the N-terminus of H2A.B may somewhat compensate for the aforementioned unwrapping effect. The assembly of

SUBMITTER: Peng J 

PROVIDER: S-EPMC7362417 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature